ABSTRACT
The aim of this work was to study the metabolism of glutathione in the isolated non-filtering rat kidney. Kidneys were perfused with Krebs-Henseleit solution containing 1 mM of glutathione. The analysis of the peptide residues and their components was done in an aminoacid microanalyzer. The results showed that glutathione was significantly oxidized to a maximal concentration of 0.06 mM at end of 20 minutes (94%). Oxidized glutathione was formed showing a slight elevation in the first 20 minutes and declining thereafter, being degraded to its constituent amino acids to a final concentration of 0.05 mM (5%). The tripeptide produced glutamic acid, glycine and cysteine in increasing concentrations. The hydrolysis of glutathione allowed us to believe that gamma glutamyl transpeptidase, among other enzymes is present in the counterluminal membranes of the rat kidney contributing to the handling of glutathione. Our results open new ways to the study of glutathione metabolism.
